BRENDA - Enzyme Database show
show all sequences of 3.1.30.2

The plant S1-like nuclease family has evolved a highly diverse range of catalytic capabilities

Lesniewicz, K.; Karlowski, W.M.; Pienkowska, J.R.; Krzywkowski, P.; Poreba, E.; Plant Cell Physiol. 54, 1064-1078 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene ENDO1, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts; gene ENDO2, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts; gene ENDO4, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts; gene ENDO5, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts
Arabidopsis thaliana
Inhibitors
Inhibitors
Commentary
Organism
Structure
Zn2+
complete inhibition; complete inhibition
Arabidopsis thaliana
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates at pH 8.0; activates at pH 8.0; activates at pH 8.0, preferred divalent cation
Arabidopsis thaliana
Mn2+
activates; activates; activates, highly activating divalent cation
Arabidopsis thaliana
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+; metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+; the enzyme activity is not affected by Mg2+ or Fe2+; the enzyme activity is not affected by Mg2+ or Fe2+
Arabidopsis thaliana
Zn2+
dependent on; dependent on, Zn2+-dependent activity of the enzyme can be strongly enhanced by the Ca2+
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Arabidopsis thaliana
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
?
-
-
-
additional information
Arabidopsis thaliana
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
?
-
-
-
additional information
Arabidopsis thaliana
no activity by isozyme ENDO5 on ssDNA or dsDNA
?
-
-
-
additional information
Arabidopsis thaliana
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
F4JJL0
gene ENDO4
-
Arabidopsis thaliana
F4JJL3
gene ENDO5
-
Arabidopsis thaliana
Q9C9G4
cf. EC 3.1.30.1; gene ENDO2
-
Arabidopsis thaliana
Q9SXA6
cf. EC 3.1.30.1; gene ENDO1
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
endosperm
;
Arabidopsis thaliana
-
flower
expression of ENDO1 is associated with flower development, expression in stamen, sepal and petal
Arabidopsis thaliana
-
additional information
in late endosperm the decrease in isozyme ENDO2 is accompanied by a significant increase in isozyme ENDO1 nucleases; in late endosperm the decrease in isozyme ENDO2 is accompanied by a significant increase in isozyme ENDO1 nucleases
Arabidopsis thaliana
-
petal
-
Arabidopsis thaliana
-
seed
; high level of ENDO2 transcription is maintained specifically in chalazal endosperm from the preglobular to the linear cotyledon stage and rapidly decreases at later stages of seed development
Arabidopsis thaliana
-
seedling
-
Arabidopsis thaliana
-
sepal
-
Arabidopsis thaliana
-
stamen
-
Arabidopsis thaliana
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
730587
Arabidopsis thaliana
?
-
-
-
-
additional information
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
730587
Arabidopsis thaliana
?
-
-
-
-
additional information
no activity by isozyme ENDO5 on ssDNA or dsDNA
730587
Arabidopsis thaliana
?
-
-
-
-
additional information
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
730587
Arabidopsis thaliana
?
-
-
-
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
isozyme ENDO5 is active in the neutral buffer and less efficiently in the acidic buffer; optimal activity at acidic pH; optimal activity at neutral pH; optimal activity at neutral pH
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ENDO1, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts
Arabidopsis thaliana
gene ENDO2, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts
Arabidopsis thaliana
gene ENDO5, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts
Arabidopsis thaliana
gene ENDO4, DNA and amino acid sequence determination and analysis, recombinant transient overexpression in Arabidosis thaliana leaf protoplasts
Arabidopsis thaliana
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Zn2+
complete inhibition
Arabidopsis thaliana
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates at pH 8.0, preferred divalent cation
Arabidopsis thaliana
Ca2+
activates at pH 8.0
Arabidopsis thaliana
Mn2+
activates
Arabidopsis thaliana
Mn2+
activates, highly activating divalent cation
Arabidopsis thaliana
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
Arabidopsis thaliana
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
Arabidopsis thaliana
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
Arabidopsis thaliana
Zn2+
dependent on, Zn2+-dependent activity of the enzyme can be strongly enhanced by the Ca2+
Arabidopsis thaliana
Zn2+
dependent on
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Arabidopsis thaliana
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
?
-
-
-
additional information
Arabidopsis thaliana
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
?
-
-
-
additional information
Arabidopsis thaliana
no activity by isozyme ENDO5 on ssDNA or dsDNA
?
-
-
-
additional information
Arabidopsis thaliana
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
endosperm
-
Arabidopsis thaliana
-
flower
expression of ENDO1 is associated with flower development, expression in stamen, sepal and petal
Arabidopsis thaliana
-
additional information
in late endosperm the decrease in isozyme ENDO2 is accompanied by a significant increase in isozyme ENDO1 nucleases
Arabidopsis thaliana
-
petal
-
Arabidopsis thaliana
-
seed
-
Arabidopsis thaliana
-
seed
high level of ENDO2 transcription is maintained specifically in chalazal endosperm from the preglobular to the linear cotyledon stage and rapidly decreases at later stages of seed development
Arabidopsis thaliana
-
seedling
-
Arabidopsis thaliana
-
sepal
-
Arabidopsis thaliana
-
stamen
-
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
730587
Arabidopsis thaliana
?
-
-
-
-
additional information
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
730587
Arabidopsis thaliana
?
-
-
-
-
additional information
no activity by isozyme ENDO5 on ssDNA or dsDNA
730587
Arabidopsis thaliana
?
-
-
-
-
additional information
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
730587
Arabidopsis thaliana
?
-
-
-
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
optimal activity at neutral pH
Arabidopsis thaliana
additional information
-
optimal activity at acidic pH
Arabidopsis thaliana
additional information
-
isozyme ENDO5 is active in the neutral buffer and less efficiently in the acidic buffer
Arabidopsis thaliana
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the plant S1-like nucleases class of enzymes. Different members of this family are characterized by a surprisingly large variety of catalytic properties, nucleolytic activities of all Arabidopsis thaliana S1-like paralogues, overview. In addition to Zn2+-dependent enzymes, this family also comprises nucleases activated by Ca2+ and Mn2+, which implies that the apparently well-known S1 nuclease active site in plant nucleases is able to cooperate with different activatory ions. Particular members of this class differ in their optimum pH value and substrate specificity. Plant representatives of this family evolve toward an increase in catalytic diversity. Phylogenetic analysis, overview; the enzyme belongs to the plant S1-like nucleases class of enzymes. Different members of this family are characterized by a surprisingly large variety of catalytic properties, nucleolytic activities of all Arabidopsis thaliana S1-like paralogues, overview. In addition to Zn2+-dependent enzymes, this family also comprises nucleases activated by Ca2+ and Mn2+, which implies that the apparently well-known S1 nuclease active site in plant nucleases is able to cooperate with different activatory ions. Particular members of this class differ in their optimum pH value and substrate specificity. Plant representatives of this family evolve toward an increase in catalytic diversity. Phylogenetic analysis, overview; the enzyme belongs to the plant S1-like nucleases class of enzymes. Different members of this family are characterized by a surprisingly large variety of catalytic properties, nucleolytic activities of all Arabidopsis thaliana S1-like paralogues, overview. In addition to Zn2+-dependent enzymes, this family also comprises nucleases activated by Ca2+ and Mn2+, which implies that the apparently well-known S1 nuclease active site in plant nucleases is able to cooperate with different activatory ions. Particular members of this class differ in their optimum pH value and substrate specificity. Plant representatives of this family evolve toward an increase in catalytic diversity. Phylogenetic analysis, overview; the enzyme belongs to the plant S1-like nucleases class of enzymes. Different members of this family are characterized by a surprisingly large variety of catalytic properties, nucleolytic activities of all Arabidopsis thaliana S1-like paralogues, overview. In addition to Zn2+-dependent enzymes, this family also comprises nucleases activated by Ca2+ and Mn2+, which implies that the apparently well-known S1 nuclease active site in plant nucleases is able to cooperate with different activatory ions. Particular members of this class differ in their optimum pH value and substrate specificity. Plant representatives of this family evolve toward an increase in catalytic diversity. Phylogenetic analysis, overview
Arabidopsis thaliana
physiological function
involvement of isozyme ENDO1 in endosperm senescence. Plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death; plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death; plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death; plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the plant S1-like nucleases class of enzymes. Different members of this family are characterized by a surprisingly large variety of catalytic properties, nucleolytic activities of all Arabidopsis thaliana S1-like paralogues, overview. In addition to Zn2+-dependent enzymes, this family also comprises nucleases activated by Ca2+ and Mn2+, which implies that the apparently well-known S1 nuclease active site in plant nucleases is able to cooperate with different activatory ions. Particular members of this class differ in their optimum pH value and substrate specificity. Plant representatives of this family evolve toward an increase in catalytic diversity. Phylogenetic analysis, overview
Arabidopsis thaliana
physiological function
involvement of isozyme ENDO1 in endosperm senescence. Plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
Arabidopsis thaliana
physiological function
plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
Arabidopsis thaliana
Other publictions for EC 3.1.30.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
730531
Filimonova
-
Some features of hydrolysis of ...
Serratia marcescens
OnLine J. Biol. Sci.
14
179-185
2014
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730764
Yu
Mung bean nuclease treatment i ...
Vigna radiata
PLoS ONE
9
e103491
2014
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1
1
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730587
Lesniewicz
The plant S1-like nuclease fam ...
Arabidopsis thaliana
Plant Cell Physiol.
54
1064-1078
2013
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1
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1
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4
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4
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4
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8
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12
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14
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4
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4
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2
8
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730959
Romanova
The effects of addition of mon ...
Serratia marcescens
ScientificWorldJournal
2012
454176
2012
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5
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1
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2
2
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695826
Li
A fluorescent, genetically eng ...
Serratia marcescens
Appl. Microbiol. Biotechnol.
82
749-756
2009
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1
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699775
Chen
Advantage of being a dimer for ...
Serratia marcescens
J. Phys. Chem. B
113
511-521
2009
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701699
Caballero
Evaluation of the Serratia mar ...
Serratia marcescens
Anim. Biotechnol.
20
177-185
2009
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1
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677620
Hanus
The major apoptotic endonuclea ...
Homo sapiens
Apoptosis
13
377-382
2008
1
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1
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4
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698091
Anisimova
Is crab duplex-specific nuclea ...
Paralithodes camtschaticus
Gene
418
41-48
2008
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1
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14
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678425
Laquel-Robert
Identification and biochemical ...
Podospora anserina
Biochim. Biophys. Acta
1770
527-542
2007
1
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666881
Chen
Solvent participation in Serra ...
Serratia marcescens
Proteins
62
982-995
2006
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680576
Mandal
Purification and characterizat ...
Mycolicibacterium smegmatis
J. Biochem. Mol. Biol.
39
140-144
2006
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665188
Pires de Castro
-
Mechanism of DNA cleavage cata ...
Vigna radiata
Inorg. Chim. Acta
357
2579-2592
2004
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666651
Yupsanis
Purification, properties and s ...
Thinopyrum elongatum
Plant Physiol. Biochem.
42
795-802
2004
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10
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2
4
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4
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12
1
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10
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1
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1
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654944
Filimonova
Action of hexaamminecobalt on ...
Serratia marcescens
BioMetals
16
447-453
2003
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1
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655293
Berkmen
Multi-copy repression of Serra ...
Serratia marcescens
Curr. Microbiol.
44
44-48
2002
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1
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657343
Shlyapnikov
-
A comparative structure-functi ...
Serratia marcescens
Russ. J. Bioorg. Chem.
28
20-27
2002
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2
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654960
Koziolkiewicz
Stereochemistry of cleavage of ...
Serratia marcescens
Bioorg. Med. Chem.
9
2403-2409
2001
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2
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657122
Marchetti
Isolation and characterization ...
Hordeum vulgare
Planta
213
199-206
2001
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-
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1
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1
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2
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1
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2
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12
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1
1
3
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1
1
2
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1
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1
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1
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2
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12
-
1
1
3
-
1
1
2
-
-
-
-
-
-
-
135016
Shlyapnikov
Atomic structure of the Serrat ...
Serratia marcescens
Acta Crystallogr. Sect. D
56
567-572
2000
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1
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2
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1
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1
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1
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135022
Lunin
-
Extracellular endonuclease of ...
Serratia marcescens
Mol. Biol.
33
180-187
1999
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1
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1
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135015
Franke
Genetic engineering, productio ...
Serratia marcescens
FEBS Lett.
425
517-522
1998
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1
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2
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4
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2
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2
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135018
Kobayashi
Purification and characterizat ...
Lentinula edodes
Biosci. Biotechnol. Biochem.
59
1169-1171
1995
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-
-
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3
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1
1
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2
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1
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2
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3
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1
1
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3
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1
1
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1
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2
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3
-
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1
1
-
-
-
-
-
-
-
-
135017
Friedhoff
A procedure for renaturation a ...
Serratia marcescens
Protein Expr. Purif.
5
37-43
1994
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-
1
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2
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3
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1
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1
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1
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1
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1
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2
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1
1
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1
-
1
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-
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-
135020
Filimonova
Kinetic studies of the Serrati ...
Serratia marcescens
Biochem. Mol. Biol. Int.
33
1229-1236
1994
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-
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4
-
1
1
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2
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1
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2
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4
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1
1
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1
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2
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-
-
135021
Pedersen
Characterization of Serratia m ...
Serratia marcescens
Biochim. Biophys. Acta
1202
13-21
1993
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-
1
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3
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3
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2
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1
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3
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2
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-
135014
Grafi
-
Characterization of S1/mung-be ...
Nicotiana tabacum, Petunia x hybrida, Solanum lycopersicum, Triticum monococcum
Plant Sci.
74
107-114
1991
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-
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8
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4
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4
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8
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8
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8
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4
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8
-
-
8
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-
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-
-
-
-
135019
Bannikova
Two isoforms of Serratia marce ...
Serratia marcescens
Biochem. Int.
24
813-822
1991
-
-
-
1
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1
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2
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1
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1
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1
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1
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1
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1
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1
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-
1
-
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-
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-
-
-
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-
-
-
95075
Brown
Biochemical properties and hor ...
Hordeum vulgare
Eur. J. Biochem.
168
357-364
1987
-
-
-
-
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3
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3
2
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4
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1
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1
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5
1
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3
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3
2
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1
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1
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5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
135010
Sawicka
-
Membrane-bound nucleolytic act ...
Zea mays
Phytochemistry
26
59-63
1987
-
-
-
-
-
-
-
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2
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1
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1
1
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9
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1
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2
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1
1
-
9
-
-
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1
-
-
-
-
-
-
-
-
-
135012
Varlamov
Ligand-exchange chromatography ...
Serratia marcescens
J. Chromatogr.
364
215-223
1986
-
-
-
-
-
-
-
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3
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1
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3
1
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1
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1
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3
1
-
1
-
-
-
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-
-
-
-
-
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-
-
95082
Imagawa
Purification and characterizat ...
Camellia sinensis
Agric. Biol. Chem.
46
1261-1269
1982
-
-
-
-
-
-
8
-
-
1
2
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-
1
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1
-
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-
1
1
4
-
2
1
2
-
2
1
1
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-
-
8
-
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1
2
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1
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-
1
1
4
-
2
1
2
-
2
1
1
-
-
-
-
-
-
-
134499
Pietrzak
Purification and properties of ...
Hordeum vulgare
Biochim. Biophys. Acta
614
102-112
1980
-
-
-
-
-
-
7
-
-
1
1
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3
-
-
1
-
-
1
1
-
2
-
-
-
-
-
4
1
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-
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-
-
-
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-
-
7
-
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-
1
1
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1
-
1
1
-
2
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
135008
Sasakuma
-
Partial purification and prope ...
Hordeum vulgare
Phytochemistry
18
1873-1874
1979
-
-
-
-
-
-
3
-
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1
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1
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1
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1
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3
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-
-
-
-
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-
-
-
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-
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3
-
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-
-
1
-
-
-
-
1
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
135011
Oleson
An extracellular nuclease from ...
Nicotiana tabacum
Biochim. Biophys. Acta
366
89-100
1974
-
-
-
-
-
-
1
-
1
1
1
-
-
1
-
-
1
-
-
1
-
-
4
-
-
-
-
-
3
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
1
1
-
-
-
-
1
-
1
-
-
4
-
-
-
-
-
3
3
-
-
-
-
-
-
-
-
135005
Stevens
-
Studies on a nuclease from Azo ...
Azotobacter agilis
J. Biol. Chem.
235
3016-3022
1960
-
-
-
-
-
-
1
-
-
-
-
-
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1
-
-
1
-
-
-
1
-
6
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
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1
-
-
1
-
6
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
135006
Stevens
-
Studies on a nuclease from Azo ...
Azotobacter agilis
J. Biol. Chem.
235
3023-3027
1960
1
-
-
-
-
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1
-
-
1
-
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1
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-
-
-
-
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-
1
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-
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-
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-
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-
1
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-
-
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1
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1
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1
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-